Please use this identifier to cite or link to this item:
https://hdl.handle.net/2440/9570
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Type: | Journal article |
Title: | A novel Apaf-1-independent putative caspase-2 activation complex |
Author: | Read, S. Baliga, B. Ekert, P. Vaux, D. Kumar, S. |
Citation: | The Journal of Cell Biology, 2002; 159(5):739-745 |
Publisher: | Rockefeller Univ Press |
Issue Date: | 2002 |
ISSN: | 0021-9525 1540-8140 |
Statement of Responsibility: | Stuart H. Read, Belinda C. Baliga, Paul G. Ekert, David L. Vaux and Sharad Kumar |
Abstract: | CVaspase activation is a key event in apoptosis execution. In stress-induced apoptosis, the mitochondrial pathway of caspase activation is believed to be of central importance. In this pathway, cytochrome c released from mitochondria facilitates the formation of an Apaf-1 apoptosome that recruits and activates caspase-9. Recent data indicate that in some cells caspase-9 may not be the initiator caspase in stress-mediated apoptosis because caspase-2 is required upstream of mitochondria for the release of cytochrome c and other apoptogenic factors. To determine how caspase-2 is activated, we have studied the formation of a complex that mediates caspase-2 activation. Using gel filtration analysis of cell lysates, we show that caspase-2 is spontaneously recruited to a large protein complex independent of cytochrome c and Apaf-1 and that recruitment of caspase-2 to this complex is sufficient to mediate its activation. Using substrate-binding assays, we also provide the first evidence that caspase-2 activation may occur without processing of the precursor molecule. Our data are consistent with a model where caspase-2 activation occurs by oligomerization, independent of the Apaf-1 apoptosome. |
Keywords: | apoptosis caspase activation apoptosome caspase-9 initiator caspase |
Description: | © The Rockefeller University Press |
DOI: | 10.1083/jcb.200209004 |
Published version: | http://dx.doi.org/10.1083/jcb.200209004 |
Appears in Collections: | Aurora harvest Medicine publications |
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